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Information on EC 1.1.1.312 - 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase
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1.1.1.312 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenaseIUBMB Comments
The enzyme does not act on unsubstituted aliphatic or aromatic aldehydes or glucose; NAD+ can replace NADP+, but with lower affinity. The enzyme was initially believed to act on 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde and produce 4-carboxy-2-hydroxy-cis,cis-muconate . However, later studies showed that the substrate is the hemiacetal form , and the product is 2-oxo-2H-pyran-4,6-dicarboxylate [2,4].
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Word Map
- 1.1.1.312
- protocatechuate
- 2-pyrone-4,6-dicarboxylate
-
4,5-dioxygenase
- lignin
-
sphingomonas
- ligab
- paucimobilis
- ochraceae
- vanillate
-
4,5-cleavage
-
hydratase
- syringate
- ecori
- dehydrogenases
-
testosteroni
- putida
- nad+
- biotechnology
- 4-oxalomesaconate
-
comamonas
- oxaloacetate
- industry
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase, chms dehydrogenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-hydroxy-4-carboxymuconate 6-semialdehyde dehydrogenase
-
-
-
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2-hydroxy-4-carboxymuconate-6-semialdehyde dehydrogenase
4-carboxy-2-hydroxy-cis,cis-muconate-6-semialdehyde:NADP+ oxidoreductase
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-
-
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4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase
alpha-hydroxy-gamma-carboxymuconic epsilon-semialdehyde dehydrogenase
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-
-
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CHMS dehydrogenase
CHMS hydrolase
dehydrogenase, 2-hydroxy-4-carboxymuconate 6-semialdehyde
-
-
-
-
EC 1.2.1.45
-
-
formerly
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2-hydroxy-4-carboxymuconate-6-semialdehyde dehydrogenase
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-
-
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4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP+ = 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H+
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP+ = 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H+
ordered bi-bi mechanism
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4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP+ = 2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
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-
-
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reduction
reduction
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-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal:NADP+ 2-oxidoreductase
The enzyme does not act on unsubstituted aliphatic or aromatic aldehydes or glucose; NAD+ can replace NADP+, but with lower affinity. The enzyme was initially believed to act on 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde and produce 4-carboxy-2-hydroxy-cis,cis-muconate [1]. However, later studies showed that the substrate is the hemiacetal form [3], and the product is 2-oxo-2H-pyran-4,6-dicarboxylate [2,4].
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CAS REGISTRY NUMBER
COMMENTARY
67272-39-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NAD+
4-carboxy-2-hydroxy-cis,cis-muconate + NADH
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+ + H2O
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH + 2 H+
4-carboxy-2-hydroxymuconate semialdehyde + NADP+
2-pyrone-4,6-dicarboxylic acid + NADPH + H2O
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP+
2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H+
-
-
-
?
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NAD+
4-carboxy-2-hydroxy-cis,cis-muconate + NADH
-
-
-
-
?
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NAD+
4-carboxy-2-hydroxy-cis,cis-muconate + NADH
-
NAD+ is less effective than NADP+
-
-
?
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NAD+
4-carboxy-2-hydroxy-cis,cis-muconate + NADH
-
NAD+ is less effective than NADP+
-
-
?
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NAD+
4-carboxy-2-hydroxy-cis,cis-muconate + NADH
-
-
-
-
?
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NAD+
4-carboxy-2-hydroxy-cis,cis-muconate + NADH
-
-
-
-
?
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH
-
-
following intramolecular dehydrogenation to the lactone 2-pyrone-4,6-dicarboxylic acid
?
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH
-
-
following intramolecular dehydrogenation to the lactone 2-pyrone-4,6-dicarboxylic acid, it is not clear whether the lactonization occurs enzymatically or nonenzymatically
?
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH
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or NAD+
-
?
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH
-
NAD+ is less effective than NADP+
-
-
?
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH
-
NAD+ is less effective than NADP+
-
-
?
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH
-
-
following intramolecular dehydrogenation to the lactone 2-pyrone-4,6-dicarboxylic acid
?
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH
-
-
following intramolecular dehydrogenation to the lactone 2-pyrone-4,6-dicarboxylic acid
?
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+ + H2O
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH + 2 H+
-
-
-
-
?
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+ + H2O
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH + 2 H+
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-
-
-
?
4-carboxy-2-hydroxymuconate semialdehyde + NADP+
2-pyrone-4,6-dicarboxylic acid + NADPH + H2O
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-
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?
4-carboxy-2-hydroxymuconate semialdehyde + NADP+
2-pyrone-4,6-dicarboxylic acid + NADPH + H2O
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?
protocatechuate + NADP+ + H2O
2-pyrone-4,6-dicarboxylic acid + NADPH + H+
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?
protocatechuate + NADP+ + H2O
2-pyrone-4,6-dicarboxylic acid + NADPH + H+
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?
additional information
?
-
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not: unsubstituted aliphatic or aromatic aldehydes
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-
?
additional information
?
-
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interaction with Blue Dextran-2000 and related dyes
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-
?
additional information
?
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2-pyrone-4,6-dicarboxylic acid may be a metabolic intermediate in the bacterial metabolism of protocatechuic acid
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+ + H2O
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH + 2 H+
4-carboxy-2-hydroxymuconate semialdehyde hemiacetal + NADP+
2-oxo-2H-pyran-4,6-dicarboxylate + NADPH + H+
-
-
-
?
additional information
?
-
-
2-pyrone-4,6-dicarboxylic acid may be a metabolic intermediate in the bacterial metabolism of protocatechuic acid
-
-
?
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+ + H2O
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH + 2 H+
-
-
-
-
?
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP+ + H2O
4-carboxy-2-hydroxy-cis,cis-muconate + NADPH + 2 H+
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-pyrone-4,6-dicarboxylic acid
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non-competitive inhibition with respect to 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde
5,5'-dithiobis(2-nitrobenzoate)
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1 h at 0.1 mM inhibits 98% of enzyme activity
methoxy Reactive Blue 2
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inhibits the enzyme non-competitively with respect to 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde and competitively with respect to NADP+
Monoiodoacetic acid
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weaker inhibitor than p-chloromercuribenzoate or HgCl2
N-ethylmaleimide
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weaker inhibitor than p-chloromercuribenzoate or HgCl2
NADH
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competitive inhibition with respect to NAD+, non-competitive inhibition with respect to 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde
NADPH
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competitive inhibition with respect to NADP, non-competitive inhibition with respect to 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde
Reactive blue 2
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inhibits the enzyme non-competitively with respect to 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde and competitively with respect to NADP+
Reactive Blue 4
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inhibits the enzyme non-competitively with respect to 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde and competitively with respect to NADP+
additional information
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not: various metal ions, metal chelating reagents, reducing reagents
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p-chloromercuribenzoate
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1 h at 0.01 mM inhibits 78% of enzyme activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Lubrol
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the enzyme activity increases in a sigmoidal manner with increasing concentrations, minimum concentration necessary for the increase of enzyme activity is higher than 0.05 mM, effectively eliminates the dye inhibition
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde
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in the presence of 0.110 mM NADP+
0.0206
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde
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in the presence of NAD+
0.026
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde
-
in the presence of NADP+
0.056
4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde
-
in the presence of 0.110 mM NAD+
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0002
methoxy Reactive Blue 2
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coenzyme NADP+, similar value with coenzyme NAD+
0.0045
Reactive Blue 4
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coenzyme NADP+, similar value with coenzyme NAD+
0.0002
Reactive blue 2
-
coenzyme NADP+, similar value with coenzyme NAD+
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
fermenter condition for production of 2-pyrone-4,6-dicarboxylic acid, PDC
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (508 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
67000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
in tobacco leaves, transient expression of bacterial feedback-resistant 3-deoxy-D-arabinoheptulosonate 7-phosphate synthase (AroG) and 3-dehydroshikimate dehydratase (QsuB) produces high titers of protocatechuate (PCA), which is in turn efficiently converted into 2-pyrone-4,6-dicarboxylic acid (PDC) upon co-expression of PCA 4,5-dioxygenase (PmdAB) and 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase (PmdC) derived from Comamonas testosteroni. Stable expression of AroG in Arabidopsis thaliana in a genetic background containing the QsuB gene enhances PCA content in plant biomass, presumably via an increase of the carbon flux through the shikimate pathway. Introducing AroG and the PDC biosynthetic genes (PmdA, PmdB, and PmdC) into the Arabidopsis QsuB background, or introducing the five genes (AroG, QsuB, PmdA, PmdB, and PmdC) stacked on a single construct into wild-type plants, results in PDC titers of about 1% and about 3% dry weight in plant biomass, respectively. Consistent with previous studies of plants expressing QsuB, all PDC producing lines show strong reduction in lignin content in stems. This low lignin trait is accompanied with improvements of biomass saccharification efficiency due to reduced cell wall recalcitrance to enzymatic degradation. Importantly, most transgenic lines show no reduction in biomass yields
additional information
-
in tobacco leaves, transient expression of bacterial feedback-resistant 3-deoxy-D-arabinoheptulosonate 7-phosphate synthase (AroG) and 3-dehydroshikimate dehydratase (QsuB) produces high titers of protocatechuate (PCA), which is in turn efficiently converted into 2-pyrone-4,6-dicarboxylic acid (PDC) upon co-expression of PCA 4,5-dioxygenase (PmdAB) and 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase (PmdC) derived from Comamonas testosteroni. Stable expression of AroG in Arabidopsis thaliana in a genetic background containing the QsuB gene enhances PCA content in plant biomass, presumably via an increase of the carbon flux through the shikimate pathway. Introducing AroG and the PDC biosynthetic genes (PmdA, PmdB, and PmdC) into the Arabidopsis QsuB background, or introducing the five genes (AroG, QsuB, PmdA, PmdB, and PmdC) stacked on a single construct into wild-type plants, results in PDC titers of about 1% and about 3% dry weight in plant biomass, respectively. Consistent with previous studies of plants expressing QsuB, all PDC producing lines show strong reduction in lignin content in stems. This low lignin trait is accompanied with improvements of biomass saccharification efficiency due to reduced cell wall recalcitrance to enzymatic degradation. Importantly, most transgenic lines show no reduction in biomass yields
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from the cell extract of Escherichia coli, using POROS polyethyleneimine anion-exchange chromatography, POROS quaternized PI anion-exchange chromatography and POROS phenylether hydrophobic-interaction chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase gene ligC expressed in Escherichia coli
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coexpression with protocatechuate 4,5-dioxygenase in Pseudomonas putida PpY1100
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gene pmdC, transient recombinant expression of the enzyme in Nicotiana benthamiana, coexpression with PmdA and, PmdB from Comamonas testosteroni, stable expression of enzymes PmdA, PmdB, and PmdC from Comamonas testosteroni in Arabidopsis thaliana, coexpression with 3-dehydroshikimate dehydratase (QsuB). The metabolic pathway is implemented in the Arabidopsis thaliana ecotype Columbia plastids to produce 2-pyrone-4,6-dicarboxylic acid (PDC), overview
into the pKT230MC vector for expression in Pseudomonas putida PpY1100 and into pUC119 for DNA amplification in Escherichia coli DH5alpha
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
industry
biotechnology
-
production of 2-pyrone-4,6-dicarboxylic acid from protocatechuate as a precursor for biopolymers
biotechnology
engineering plants with the proposed de-novo PDC pathway provides an avenue to enrich biomass with a value-added co-product while simultaneously improving biomass quality for the supply of fermentable sugars. Implementing this strategy into bioenergy crops has the potential to support existing microbial fermentation approaches that exploit lignocellulosic biomass feedstocks for PDC production
biotechnology
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production of 2-pyrone-4,6-dicarboxylic acid from protocatechuate as a precursor for biopolymers
-
industry
-
the authors focus on the metabolic intermediate 2-pyrone-4,6-dicarboxylic acid as a potential raw material for novel, bio-based polymers
industry
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the authors focus on the metabolic intermediate 2-pyrone-4,6-dicarboxylic acid as a potential raw material for novel, bio-based polymers
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maruyama, K.
Interaction of 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase with Reactive Blue 2 and related dyes
J. Biochem.
103
714-721
1988
Pseudomonas straminea
brenda
Maruyama, K.
Isolation and identification of the reaction product of alpha-hydroxy-gamma-carboxymuconic epsilon-semialdehyde dehydrogenase
J. Biochem.
86
1671-1677
1979
Pseudomonas straminea
brenda
Maruyama, K.; Ariga, N.; Tsuda, M.; Deguchi, K.
Purification and properties of alpha-hydroxy-gamma-carboxymuconic epsilon-semialdehyde dehydrogenase
J. Biochem.
83
1125-1134
1978
Pseudomonas straminea
brenda
Masai, E.; Momose, K.; Hara, H.; Nisihikawa, S.; Katayama, Y.; Fukuda, M.
Genetic and biochemical characterization of 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase and its role in the protocatechuate 4,5-cleavage pathway in Sphingomonas paucimobilis SYK-6
J. Bacteriol.
182
6651-6658
2000
Sphingomonas paucimobilis, Sphingomonas paucimobilis SYK6
brenda
Maruyama, K.; Shibayama, T.; Ichikawa, A.; Sakou, Y.; Yamada, S.; Sugisaki, H.
Cloning and characterization of the genes encoding enzymes for the protocatechuate meta-degradation pathway of Pseudomonas ochraceae NGJ1
Biosci. Biotechnol. Biochem.
68
1434-1441
2004
Pseudomonas straminea, Pseudomonas straminea NGJ1
brenda
Otsuka, Y.; Nakamura, M.; Shigehara, K.; Sugimura, K.; Masai, E.; Ohara, S.; Katayama, Y.
Efficient production of 2-pyrone 4,6-dicarboxylic acid as a novel polymer-based material from protocatechuate by microbial function
Appl. Microbiol. Biotechnol.
71
608-614
2006
Sphingomonas paucimobilis, Sphingomonas paucimobilis SYK-6
brenda
Lin, C.Y.; Vuu, K.M.; Amer, B.; Shih, P.M.; Baidoo, E.E.K.; Scheller, H.V.; Eudes, A.
In-planta production of the biodegradable polyester precursor 2-pyrone-4,6-dicarboxylic acid (PDC) stacking reduced biomass recalcitrance with value-added co-product
Metab. Eng.
66
148-156
2021
Comamonas testosteroni (Q93PS4), Comamonas testosteroni
brenda
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